Crystallization and Preliminary X-ray Analysis of a Thiol-Activated Cytolysin

FEBS Lett. 1996 Nov 18;397(2-3):290-2. doi: 10.1016/s0014-5793(96)01200-8.

Abstract

We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin O, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C222(1) with cell dimensions of a = 47.8 A, b = 182.0 A and c = 175.5 A and the crystals diffract to beyond 2.5 A resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P222(1) with unit cell dimensions a = 47.1 A, b = 166.1 A and c = 214.0 A and with diffraction observed to 2.4 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Toxins / chemistry*
  • Clostridium perfringens*
  • Crystallization
  • Crystallography, X-Ray
  • Hemolysin Proteins / chemistry*
  • Solvents
  • Sulfhydryl Compounds / pharmacology

Substances

  • Bacterial Toxins
  • Hemolysin Proteins
  • Solvents
  • Sulfhydryl Compounds
  • Clostridium perfringens theta-toxin